A0A8G2J172 · A0A8G2J172_RHILV

Function

function

Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes successive additions of L-glutamate to tetrahydrofolate or 10-formyltetrahydrofolate or 5,10-methylenetetrahydrofolate, leading to folylpolyglutamate derivatives.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Pathway

Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 2/2.
Cofactor biosynthesis; tetrahydrofolylpolyglutamate biosynthesis.

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionATP binding
Molecular Functiondihydrofolate synthase activity
Molecular Functionmetal ion binding
Molecular Functiontetrahydrofolylpolyglutamate synthase activity
Biological Processfolic acid biosynthetic process
Biological Processtetrahydrofolate biosynthetic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Dihydrofolate synthase/folylpolyglutamate synthase
  • EC number
  • Alternative names
    • Folylpoly-gamma-glutamate synthetase-dihydrofolate synthetase
    • Folylpolyglutamate synthetase
    • Tetrahydrofolylpolyglutamate synthase

Gene names

    • ORF names
      E0H31_17640

Organism names

  • Taxonomic identifier
  • Strain
    • SPF4F3
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Rhizobiaceae > Rhizobium/Agrobacterium group > Rhizobium

Accessions

  • Primary accession
    A0A8G2J172

Proteomes

Subcellular Location

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain57-231Mur ligase central
Domain307-422Mur ligase C-terminal

Sequence similarities

Belongs to the folylpolyglutamate synthase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    432
  • Mass (Da)
    45,915
  • Last updated
    2022-01-19 v1
  • MD5 Checksum
    DD4173EBE172802724A9306D1F8648AC
MSSHIESERLSNSLAELDQLTNWERRPRGDMRVDLEPMGDLARRLGDPQNSFRIVHVAGTKGKGSTCALIEAGLLRAGFSVGRYASPHVMHITERVSIDGSPVGEERLADALGAALAAFKDGRREATGGQGATWFDILTVSAFLIFRSERVEWAVLETGLGGRWDSTNIVQSDVAVITNIDLEHTEILGKTRAAIAFEKAGIIKRGATVVTLLPEADEAGAVISARAEELGSAVRRPTVPADATIEQRNVALAGAVLDVLGKMGVMTKGASAMPEPLGVQLLDPSTIEAARLPGRLEKFAVDTSHGDNAKVNVVLDGAHVPFNLAAVLSDLSQEEKYRAPCIAVMSIAEDKDAAGLLSTMTRQDMSIIFTTVGARSRSPEQLKTIADTIGLLSIVMLDPLEAYQEALAGATESGAWVLVTGSLYLVGIIRSA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SJLU01000008
EMBL· GenBank· DDBJ
TBX92514.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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